Mitochondrial functionality and beef colour: A review of recent research

The bright-red colour of meat that consumers prefer depends on the depth of oxygen diffusion into the tissue and myoglobin oxygenation. Interestingly, both processes are influenced by mitochondrial activity in postmortem muscle. The transition of muscle metabolism from aerobic to anaerobic pathways affects various cellular processes including mitochondrial functionality. Numerous studies report that even with compromised structure, mitochondria continue to influence postmortem beef colour via oxygen consumption and metmyoglobin reducing activity. Hence, an in-depth understanding of the pre- and post-harvest factors affecting mitochondrial functionality can significantly enhance existing knowledge of meat colour and colour stability. Several comprehensive reviews have discussed the biochemical factors affecting meat colour, but there are only a few that have sections on the impact of mitochondria on beef colour. Furthermore, advancement of high-throughput techniques such as metabolomics and proteomics has enabled researchers to elucidate metabolite and protein changes related to mitochondria. Therefore, the objective of this review is to provide an overview on the role of mitochondria in beef colour, with a focus on recent advances in mitochondrial research, oxygen consumption, and metmyoglobin reducing ability.Keywords: Myoglobin, metmyoglobin reducing activity, meat colour, metabolomics, oxygen consumption, proteomic

Intramuscular variation in mitochondrial functionality of beef semimembranosus

Intramuscular color stability variations in beef semimembranosus have been reported previously. Mitochondria remain biochemically active in postmortem muscle and can influence fresh beef color stability. However, the role of mitochondrial functionality in intramuscular color variations in beef semimembranosus is yet to be examined. We examined the functionality of mitochondria isolated from outside (OSM) and inside (ISM) regions of beef semimembranosus. Semimembranosus muscles (n = 5) were collected from inside rounds of beef carcasses 48 h post-mortem and were separated to OSM and ISM steaks. Color attributes were evaluated instrumentally and biochemically on days 0 and 4 of retail display, whereas mitochondrial oxygen consumption rate (OCR) was measured on day 0 using succinate as substrate using steaks frozen during fabrication. Mitochondrial OCR was significantly greater in OSM than in ISM on day 0. The ISM steaks exhibited significantly greater redness (a* value) than OSM steaks on day 0, but OSM steaks had significantly greater redness than the ISM counterparts on day 4. During retail display, ISM steaks exhibited greater lightness (L* value) than OSM steaks. However, OSM demonstrated significantly greater color stability and metmyoglobin reducing activity than ISM throughout the display. The observed differences in mitochondrial OCR between ISM and OSM steaks indicated that mitochondrial biochemistry possibly contributes to the intramuscular color variations in beef semimembranosus.Keywords: Beef color, color stability, mitochondria, semimembranosu

Ractopamine-induced changes in sarcoplasmic proteome profile of post-rigor pork semimembranosus muscle

Ractopamine is a beta-adrenergic agonist that increases leanness and carcass weight in finishing pigs. Our previous study observed that dietary ractopamine increased the abundance of several glycolytic enzymes in the sarcoplasmic proteome of post-rigor pork longissimus thoracis muscle. Pork semimembranosus is an economically important muscle and demonstrates differences in biochemistry compared with longissimus thoracis. Nonetheless, the effects of ractopamine on sarcoplasmic proteome of semimembranosus have not been evaluated yet. Therefore, this study examined the influence of ractopamine on sarcoplasmic proteome of post-rigor pork semimembranosus. Analyses of sarcoplasmic proteome of semimembranosus muscles from control (CON; diet without ractopamine) and ractopamine-fed (RAC; 7.4 mg/kg for 14 days followed by 10.0 mg/kg for 14 days) barrows revealed that haemoglobin subunit beta, alpha-crystallin B, and titin fragments were over-abundant in CON. In contrast, myosin light chain 1/3 and tripartite motif-containing protein 72 were over-abundant in RAC. The low abundance of haemoglobin subunit beta and alpha crystallin B in RAC could be attributed to fibre type shift (from oxidative to glycolytic) in response to ractopamine. The over-abundance of MLC 1/3 and tripartite motif-containing protein 72 in RAC could be due to the increased myofibrillar protein synthesis and muscle mass in ractopamine-fed pigs. Dietary ractopamine decreased the abundance of sarcoplasmic proteins involved in oxygen transport and chaperone activity, but increased the abundance of proteins involved in muscle contraction and plasma membrane repair in pork semimembranosus muscle.Keywords: Pork, ractopamine, sarcoplasmic proteome, semimembranosu

Supranutritional supplementation of vitamin E influences mitochondrial proteome profile of post-mortem longissimus lumborum from feedlot heifers

Supplementation of vitamin E improves beef colour stability by minimizing lipid oxidation-induced myoglobin oxidation. Mitochondria affect myoglobin redox stability, and dietary vitamin E influences mitochondrial functionality in skeletal muscles. Nonetheless, the influence of vitamin E on the mitochondrial proteome of beef skeletal muscles has yet to be  investigated. Therefore, the objective of this study was to examine the effect of dietary vitamin E on mitochondrial proteome of post-mortem beef longissimus lumborum (LL) muscle. Beef LL muscle samples (24 hours post-mortem) were obtained from the carcasses of nine (n = 9) vitamin E-fed (VITE) (1000 IU vitamin E for 89 days) and nine (n = 9) control (CONT) (diet without supplemental vitamin E) heifers. The mitochondrial proteome was analysed using two-dimensional gel electrophoresis and mass spectrometry, and nine differentially abundant spots were identified. All the differentially abundant spots were over-abundant in CONT, and the proteins were electron transport chain enzymes (NADH dehydrogenase iron-sulphur protein 8, NADH dehydrogenase flavoprotein 2, and cytochrome c oxidase subunit 5B), metabolic enzymes (succinate-CoA ligase (ADP-forming) subunit beta; dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; pyruvate dehydrogenase protein X component), and enzymes involved in ATP regeneration (creatine kinase S-type). The low abundance of these proteins in VITE may decrease mitochondrial activity, resulting in low oxidative activity. These findings suggest that the strong antioxidant activity of vitamin E leads to less expression of mitochondrial oxidative enzymes in beef skeletal muscles.Keywords: Beef colour, lipid oxidation, mitochondrial enzyme

Ractopamine-induced changes in the proteome of post-mortem beef longissimus lumborum muscle

Ractopamine is a beta-adrenergic agonist that is approved for use in beef cattle, pigs and turkeys as a repartitioning agent to increase lean muscle deposition and decrease lipogenesis. Although the effects of dietary ractopamine on the proteome profile of post-mortem pork muscles have been examined, its influence on beef muscle proteome has not been studied. Therefore, the objective of this study was to examine the effect of ractopamine on the proteome profile of post-mortem beef longissimus lumborum (LL) muscle. LL muscle samples were obtained from the carcasses of six (n = 6) steers fed ractopamine (RAC; 400 mg ractopamine hydrochloride for 28 days) and six (n = 6) steers fed no ractopamine (CON). The muscle proteome was analysed using two-dimensional gel electrophoresis and tandem mass spectrometry. Five differentially abundant spots were identified, and all the spots were over-abundant in RAC. The identified proteins were involved in muscle structure development (F-actin-capping protein subunit beta-2; PDZ and LIM domain protein-3), chaperone activity (heat shock protein beta-1), oxygen transport (myoglobin), and glycolysis (L-lactate dehydrogenase A chain). These results suggested that dietary ractopamine could influence the abundance of enzymes associated with muscle development and muscle fibre type shift in beef LL muscle.Keywords: growth promotants, meat quality, proteomic

The Gribov-Zwanziger action in the presence of the gauge invariant, nonlocal mass operator Tr∫d4xFμν(D2)−1FμνTr \int d^4x F_{\mu\nu} (D^2)^{-1} F_{\mu\nu} in the Landau gauge

We prove that the nonlocal gauge invariant mass dimension two operator $F_{\mu\nu} (D^2)^{-1} F_{\mu\nu}$ can be consistently added to the Gribov-Zwanziger action, which implements the restriction of the path integral's domain of integration to the first Gribov region when the Landau gauge is considered. We identify a local polynomial action and prove the renormalizability to all orders of perturbation theory by employing the algebraic renormalization formalism. Furthermore, we also pay attention to the breaking of the BRST invariance, and to the consequences that this has for the Slavnov-Taylor identity.Comment: 30 page

Gravitation search algorithm: Application to the optimal IIR filter design

This paper presents a global heuristic search optimization technique known as Gravitation Search Algorithm (GSA) for the design of 8th order Infinite Impulse Response (IIR), low pass (LP), high pass (HP), band pass (BP) and band stop (BS) filters considering various non-linear characteristics of the filter design problems. This paper also adopts a novel fitness function in order to improve the stop band attenuation to a great extent. In GSA, law of gravity and mass interactions among different particles are adopted for handling the non-linear IIR filter design optimization problem. In this optimization technique, searcher agents are the collection of masses and interactions among them are governed by the Newtonian gravity and the laws of motion. The performances of the GSA based IIR filter designs have proven to be superior as compared to those obtained by real coded genetic algorithm (RGA) and standard Particle Swarm Optimization (PSO). Extensive simulation results affirm that the proposed approach using GSA outperforms over its counterparts not only in terms of quality output, i.e., sharpness at cut-off, smaller pass band ripple, higher stop band attenuation, but also the fastest convergence speed with assured stability

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Not AvailableOur objectives were to determine the effects of lactate and modified atmosphere packaging on raw surface color, lipid oxidation, and internal cooked color of ground beef patties. Eight chubs (85% lean) were divided in half and each half was either assigned to the control (no lactate) or mixed with 2.5% lactate (w/w). Following treatment, patties were prepared and packaged in either vacuum, PVC (atmospheric oxygen level), high-oxygen (80% O2 + 20% CO2), or 0.4% CO (30% CO2 + 69.6% N2) and stored for 0, 2, or 4 days at 2 °C. After storage, raw surface color and lipid oxidation were measured and patties were cooked to either 66 °C or 71 °C. Lactate improved (p 0.05) on the a∗ values and visual color scores of patties in 0.4% CO. Lactate decreased (p 0.05) on premature browning, whereas patties packaged in high-oxygen demonstrated premature browning. Conversely, cooked patties in 0.4% CO and vacuum were more red (p < 0.05) than both high-oxygen and PVC-packaged patties. Although lactate improved raw color stability, it did not minimize premature browning in cooked ground beef patties.Not Availabl